STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
purLPhosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain protein; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and [...] (713 aa)    
Predicted Functional Partners:
purQ
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain protein; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interac [...]
 0.999
purS
Phosphoribosylformylglycinamidine (FGAM) synthase, PurS component; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and i [...]
 
 0.999
purD
Phosphoribosylamine-glycine ligase; COG0151; Belongs to the GARS family.
  
 0.997
purM
Phosphoribosylformylglycinamidine cyclo-ligase; COG0150.
 
 
0.997
purT
Phosphoribosylglycinamide formyltransferase 2; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family.
  
 
 0.991
purE
Phosphoribosylaminoimidazole carboxylase catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
  
 0.990
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
 
 0.979
CL1_1601
Asparagine synthase; COG0367.
  
 
 0.979
CL1_1777
Adenylosuccinate lyase; COG0015; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
 
  
 0.972
guaAB
GMP synthase subunit B; Catalyzes the synthesis of GMP from XMP.
  
  
 0.918
Your Current Organism:
Thermococcus cleftensis
NCBI taxonomy Id: 163003
Other names: DSM 27260, KACC 17922, T. cleftensis, Thermococcus cleftensis Hensley et al. 2014, Thermococcus sp. CL1, strain CL1
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.